Evidence map›Paper›PMID 31749672›Full record

ArticleFrontiers in neuroscience2019

Different Heat Shock Proteins Bind α-Synuclein With Distinct Mechanisms and Synergistically Prevent Its Amyloid Aggregation.

Chunyu Jia, Xiaojuan Ma, Zhenying Liu, Jinge Gu, Xiang Zhang, Dan Li, Shengnan Zhang

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in neuroscience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.3field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 44 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Chunyu JiaInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Xiaojuan MaInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Zhenying LiuInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Jinge GuInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Xiang ZhangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Dan LiKey Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders (Ministry of Education), Bio-X Institutes, Shanghai Jiao Tong University, Shanghai, China.
Shengnan ZhangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.
Chinese Academy of Sciences · CNShanghai Institute of Organic Chemistry · CNShanghai Jiao Tong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Synuclein (α-Syn) forms pathological amyloid aggregates deposited in Lewy bodies and Lewy neurites in the brain of Parkinson's disease (PD) patients. Heat shock proteins (Hsps) are the major components of the cellular chaperone network, which are responsible for preventing proteins from amyloid aggregation. Different Hsps were reported to interact with α-syn. However, the underlying mechanism of the interplay between α-syn and different Hsps remains unclear. Here, by combing NMR spectroscopy, electron microscope and other biochemical approaches, we systemically investigated the interaction between α-syn and three Hsps from different families including Hsp27, HDJ1, and Hsp104. We found that all three Hsps can weakly bind to α-syn and inhibit it from amyloid aggregation. Intriguingly, different Hsps recognize distinct regions of α-syn monomer, and act synergistically in chaperoning α-syn from fibril formation in sub-stoichiometry. Our results revealed the diverse binding mechanisms employed by different Hsps to tackle α-syn, and suggested that different Hsps form a network for cooperatively chaperoning α-syn from pathological aggregation.

Indexed as

amyloid aggregationheat shock proteinParkinson’s diseaseprotein homeostasissynergistic effectα-syn

Identifiers

PMID31749672
PMCPMC6842937
OpenAlexW2985941236

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.